Cloned (Comment) | Organism |
---|---|
gene Mj1640, expression of wild-type and selenmethionine-labeled enzyme as N-terminally His-tagged protein in Escherichia coli strain Bl21(DE3) | Methanocaldococcus jannaschii |
Crystallization (Comment) | Organism |
---|---|
purified recombinant wild-type and selenmethionine-labeled DUF358/Mj1640 in complex with S-adenosyl-L-methionine, at 20°C, mixing of 0.001 ml of protein solution with 0.001 l of reservoir containing 20% PEG 3350, 25 mM NH4F, 20 mM MgCl2, 100 mM Tris, pH 7.5, X-ray diffraction structure determination and analysis at 1.4 A resolution | Methanocaldococcus jannaschii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanocaldococcus jannaschii | Q59034 | gene Mj1640 | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type and selenmethionine-labeled Mj1640 from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography and gel filtration | Methanocaldococcus jannaschii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | SAM-binding pocket Asp157 or Glu183 from its own monomer or Ser43 from the associate monomer probably plays the catalytic role for RNA methylation, RNA-binding residues and putative active site, overview | Methanocaldococcus jannaschii | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | Mj1640 forms a dimer, which is mediated by two parallel pairs of alpha-helices oriented almost perpendicular to each other | Methanocaldococcus jannaschii |
More | the enzyme shows a single domain structure consisting of eight-stranded beta-sheets sandwiched by six alpha-helices at both sides. Mj1640 has limited structural extension at its N-terminus, which is unique to this family member, structure modeling based on the crystal structure, overview | Methanocaldococcus jannaschii |
Synonyms | Comment | Organism |
---|---|---|
DUF358/Mj1640 | - |
Methanocaldococcus jannaschii |
m1-pseudouridine methyltransferase | - |
Methanocaldococcus jannaschii |
m1G | - |
Methanocaldococcus jannaschii |
M3U | - |
Methanocaldococcus jannaschii |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a SPOUT-class RNA methyltransferase and belongs to the DUF358 family. The DUF358/Mj1640 protein shows close structural relationship to Nep1, a pseudouridine-N1-specific rRNA methyltransferase | Methanocaldococcus jannaschii |